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Structure paper

TitleImproving thermostability and catalytic activity of pyranose 2-oxidase from Trametes multicolor by rational and semi-rational design
Journal, issue, pagesFebs J., Vol. 276, Page 776-792, Year 2009
Publish dateNov 26, 2007 (structure data deposition date)
AuthorsSpadiut, O. / Leitner, C. / Salaheddin, C. / Varga, B. / Vertessy, B.G. / Tan, T.C. / Divne, C. / Haltrich, D.
External linksFebs J. / PubMed:19143837
MethodsX-ray diffraction
Resolution1.7 - 2.1 Å
Structure data

PDB-3bg6:
Pyranose 2-oxidase from Trametes multicolor, E542K mutant
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-3bg7:
Pyranose 2-oxidase from Trametes multicolor, L537G mutant
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-3bly:
Pyranose 2-oxidase from Trametes multicolor, E542K/L537W
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-HOH:
WATER

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

Source
  • trametes multicolor (fungus)
KeywordsOXIDOREDUCTASE / GMC OXIDOREDUCTASE / E542K MUTANT / ROSSMANN FOLD / PHBH FOLD / HOMOTETRAMER / 8-ALPHA-(N3) HISTIDYL FLAVINYLATION / L537G MUTANT / ROSSMANFOLD / E542K/L537W THERMOSTABLE MUTANT

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